@article{ref1,
title="Interaction of duodenase with serpins from human blood serum",
journal="Russian Journal of Bioorganic Chemistry",
year="2003",
author="Popykina, N.A. and Gladysheva, I.P. and Zamolodchikova, T.S. and Larionova, N.I.",
volume="29",
number="6",
pages="550-555",
abstract="The interaction of duodenase, a new serine protease from a small group of Janus-faced proteases, with serpins, α1-protease inhibitor (α1-PI) and antichymotrypsin (ACT) from human blood serum, was studied. The stoichiometry of the inhibition process was found to be 1.2 and 1.3 mol/mol for α1-PI and ACT, respectively. The presence of a stable enzyme-inhibitory complex duodenase-α1-PI was confirmed by SDS-PAGE. The formation of the duodenase-ACT complex was not demonstrated; instead, the band of the cleaved inhibitor indicated the ACT hydrolysis. The suicide mechanism of the duodenase interaction with the human blood serpins was proved. The association rate constants (ka × 105, M-1 s-1) were 2.4 ± 0.3 × 105 for α1-PI and 3.0 ± 0.4 × 105 for ACT. These results indicate the possibility of the regulation of duodenase activity by endogenous serpins.<p /><p>Language: en</p>",
language="en",
issn="1068-1620",
doi="10.1023/B:RUBI.0000008895.66892.9a",
url="http://dx.doi.org/10.1023/B:RUBI.0000008895.66892.9a"
}